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Database: UniProt
Entry: U5RSI5_9CLOT
LinkDB: U5RSI5_9CLOT
Original site: U5RSI5_9CLOT 
ID   U5RSI5_9CLOT            Unreviewed;       466 AA.
AC   U5RSI5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   22-NOV-2017, entry version 28.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=CAETHG_0278 {ECO:0000313|EMBL:AGY74509.1};
OS   Clostridium autoethanogenum DSM 10061.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY74509.1, ECO:0000313|Proteomes:UP000017590};
RN   [1] {ECO:0000313|EMBL:AGY74509.1, ECO:0000313|Proteomes:UP000017590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY74509.1};
RX   PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA   Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA   Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT   "Comparison of single-molecule sequencing and hybrid approaches for
RT   finishing the genome of Clostridium autoethanogenum and analysis of
RT   CRISPR systems in industrial relevant Clostridia.";
RL   Biotechnol. Biofuels 7:40-40(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP006763; AGY74509.1; -; Genomic_DNA.
DR   RefSeq; WP_023161744.1; NZ_CP012395.1.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; AGY74509; AGY74509; CAETHG_0278.
DR   GeneID; 33106011; -.
DR   KEGG; cah:CAETHG_0278; -.
DR   PATRIC; fig|1341692.11.peg.269; -.
DR   OrthoDB; POG091H01QL; -.
DR   Proteomes; UP000017590; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:AGY74509.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000017590};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017590};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   466 AA;  52127 MW;  738708D3519E21A2 CRC64;
     MSKNLTKEYK YAWDKYSKKD FKILFKISDE YEKFMSKCKT ERECVKEFIL RAEKNGYKNI
     EDIMNAKSTL KAGDKFYANN KNKNLALFVI GTENMEKGMR ILGAHIDSPR LDLKQNPLYE
     DADLALFDTH YYGGIKKYQW VTLPLAIHGV VIKKDGTKVE IVIGEEDGDP VVGVSDLLVH
     LAGDQMDKKG NKVVEGEDLN VLIGSIPIED KEAKNRVKKN ILRILNDKYG IEEEDFVSAE
     LEVVPAGPAR DFGLDSSMVM AYGHDDKICA YTSFDAMMKI ENPNKTCVTL LVDKEEIGSV
     GATGMQSRFF ENTVAEVMSL CEEYSDLKLR RALTNSKMLS SDVSAAFDPN YPSVMDKNNA
     AYFGKGVVFN KYTGARGKSG CNDANPEYIA EIRNIMDKND VSWQTAELGK VDQGGGGTIA
     YILAEYNMQV IDCGIALHNM HAPWEVASKA DIYEAVKGYV AFLKEI
//
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